Abstract:The purpose of this study was to conduct further bioinformatics analysis of the five hemolysin oftreponema pallidum, and to provide evidence for the pathogenic mechanism of hemolysin family proteins in the pathogenesis oftreponema pallidum. MethodsThe general properties of the syphilis family proteins, signal peptides, glycosylation, phosphorylation sites, subcellular positions, secondary structures, functional domains, and antigen epitopes were analyzed by bioinformatic analysis methods using NCBI, BLAST, CDD, BioEdit, ExPASy, SignalP, TMHMM, MEGA, PSORTb 3.0, ABCpred andother bioinformatics analysis methods. ResultsGeneral properties of five hemolysinfamily proteinsin Treponema pallidum were predicted, Tp1037 functional domains differ from the other four. Tp0028 contains one signal peptide,Tp0027 contains one glycosylation site, all five hemolysin family proteins contain multiple phosphorylation sites and B cell and T cell epitopes. ConclusionTreponema pallidumcontains five hemolysin family protein genes,suggesting that when treponema pallidum invades the host, these gene products are highly likely to undergo their membrane-forming pore toxicity, damage the target cells, and thus cause disease.